The differing developmental timelines of phospholamban phosphorylation and Ca2+-uptake suggest separate genetic control for the synthesis of phospholamban and sarcoplasmic reticulum Ca2+-ATPase in chick hearts.
Hypothesis-generating for separate genetic control of phospholamban and SERCA; leaves open mammalian translation and clinical relevance.
Phosphorylation of phospholamban and development of reticular Ca2+ transport were studied in crude membrane preparations of embryonic, newborn and adult chick heart. Maximal phosphorylation of phospholamban by added catalytic subunit of cyclic AMP-dependent protein kinase increases from embryonic day 4-15. It decreases with further development. In the same membrane preparations active Ca2+-uptake into vesicles of sarcoplasmic reticulum rises from day 4-7 and decreases then slightly until day 20. A several-fold increase in Ca2+-transport activity occurs at the time of hatching. The data indicate separate genetic control for synthesis of phospholamban and sarcoplasmic reticulum Ca2+-ATPase.
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Will et al. (1983) studied this question.
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